ID W6R7V6_PENRF Unreviewed; 836 AA.
AC W6R7V6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Peptidase S8, subtilisin-related {ECO:0000313|EMBL:CDM37937.1};
GN ORFNames=PROQFM164_S07g000286 {ECO:0000313|EMBL:CDM37937.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37937.1};
RN [1] {ECO:0000313|EMBL:CDM37937.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM37937.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; HG792021; CDM37937.1; -; Genomic_DNA.
DR AlphaFoldDB; W6R7V6; -.
DR STRING; 1365484.W6R7V6; -.
DR OMA; AINFAYQ; -.
DR OrthoDB; 5474719at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..836
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004880426"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..617
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 621..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 836 AA; 91437 MW; AD0BE7809A858BB7 CRC64;
MRIVSGITAT LGLAGAVSAN LHPRSQETRD FFALQLDDTT SPSHIAQILG ARHEGQIGQL
DGHHTFSLPR EQTPQFDTLL NDLRTRRKLR RRSGAIGSSD DPLDKILWSH KIAPARQRLQ
KRLPPVSVPY KSLDKREDAQ AVAFRKDAMS TLGITDPIFK EQWHLINTKQ PGHDLNVTGL
WLEGITGKGV ATAVVDDGLD MDSYDLKPNY LPEGSWDFNE GLPEPRPLLL DDKHGTRCCG
EIAAAKNDVC GVGVAYDSKI AGIRILSKPI DDVDEAAAIN YAYQKNDIYS CSWGPIDDGA
TMDAPGILIK RAMVNGIQKG RGGKGSVYVF AAGNGASYGD NCNFDGYTNS IYSITVGAID
REGNHPPYSE SCSAQLVVAY SSGSGAYIHT TDVGARECSA GHGGTSAAGP LAAGSVALAL
SARPELTWRD LQYLMVETAV PVSEDDGSWQ NLPSGRKFSH DWGFGKVDTY TMVQLAKTWD
LVKPQAWFNS PWLRVHQEIP QGDRGLLSHY TVTADQLKEA NFAKLEHVTV TMNANHTRRG
DISVELRSPA GIISYLSVAR EKDVMPVGYE DWTFMSVAHW GESPIGDWSI IVKDSNVNEF
TGAFIDWRLN LWGEAADGAK QELHPLPDDH DDDHPYEDAP VATTSVTAAP TKTPAPNPDD
HHDRPVNAKP KPKPTTTNPT PIEDVKLPTS TTSNEAETPS ASSAGSGYIS SWLPTFGASK
RTQIWIYASM AMIVTFFIGL GVYFQLQRVK RRRTTAHDDY EFEMIEDEDE MQPMTGASGR
TQRRGGELYN AFAGESDEEM FSDDDDDQPY RDGLANIPEK DNGDGTSHGG PHLPKP
//
